By using polyacrylamide gel electrophoresis and biochemical straining method, malic enzyme isozyme in 10 organs of male or female Varicorhinus macrolepis were analyzed. The results showed that malic enzyme exists in heart, gonads, eyes and gills tissues in both female and male V. macrolepis. There was only one ME-2 in heart and ME-1 in eye of female fish, while there were ME-1 and ME-2 in heart and ME-2 in eyes of male fish. Ovary contained ME-1 and ME-2, while spermary only contained ME-1. In kidney and spleen tissues, malic enzyme was found only in female fish, while in muscle, malic enzyme existed only in male fish. The phenotypic of malic enzyme had obvious differences no matter in the same organ of different sexes in V. macrolepis or different organs in the same sex. But there were no differences among different individuals of the same sex. The results will provide basic data for developmental genetics, breed improvement and directed breeding of V. macrolepis, and lay a foundation for its development and protection.
[Objective] The paper aimed at researching lectins in muscles of Varicorhinus macrolepis and providing scientific basis for researching the adaptation mechanism and immune response of V.macrolepis to environment,which were advantageous for the protection and reproduction of V.macrolepis.[Method] V.macrolepis was used as test materials for the hemagglutination test by dialdehyde fixation to prove the existence of lectins in muscle crude homogenate of Varicorhinus macrolepis and study the physical and chemical characters.[Result] Lectins in muscle crude homogenate of V.macrolepis had shown hemagglutination effects on erythrocytes of six types of animals and had the maximum hemagglutination activity against rabbit erythrocytes,which belonged to the S-type lectins with optimal pH ranged from 4 to 8 and optimal temperature at 60 ℃.Results from the saccharide inhibition test had indicated that the sucrose was the only kind of saccharide which had inhibited the hemagglutination,suggesting that sucrose had played an important role in the process of recognition and aggregation of lectins.[Conclusion] It had been speculated that the optimal pH ranges for thermal sensitivity and hemagglutination activity of lectins in different types of aquatic organisms were similar.